Recombinant human EPO-R protein (Active) is a Human Fragment protein, in the 25 to 250 aa range, expressed in Baculovirus infected insect, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, FuncS.
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Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
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Receptor for erythropoietin, which mediates erythropoietin-induced erythroblast proliferation and differentiation (PubMed:10388848, PubMed:2163695, PubMed:2163696, PubMed:8662939, PubMed:9774108). Upon EPO stimulation, EPOR dimerizes triggering the JAK2/STAT5 signaling cascade (By similarity). In some cell types, can also activate STAT1 and STAT3 (PubMed:11756159). May also activate the LYN tyrosine kinase (By similarity). Isoform EPOR-T. Acts as a dominant-negative receptor of EPOR-mediated signaling.
Erythropoietin receptor, EPO-R, EPOR
Recombinant human EPO-R protein (Active) is a Human Fragment protein, in the 25 to 250 aa range, expressed in Baculovirus infected insect, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, FuncS.
pH: 7.4
Constituents: 90% PBS, 10% Glycerol (glycerin, glycerine)
Affinity purified
Receptor for erythropoietin, which mediates erythropoietin-induced erythroblast proliferation and differentiation (PubMed:10388848, PubMed:2163695, PubMed:2163696, PubMed:8662939, PubMed:9774108). Upon EPO stimulation, EPOR dimerizes triggering the JAK2/STAT5 signaling cascade (By similarity). In some cell types, can also activate STAT1 and STAT3 (PubMed:11756159). May also activate the LYN tyrosine kinase (By similarity).
Belongs to the type I cytokine receptor family. Type 1 subfamily.
On EPO stimulation, phosphorylated on C-terminal tyrosine residues by JAK2 (PubMed:11781573). The phosphotyrosine motifs are also recruitment sites for several SH2-containing proteins and adapter proteins which mediate cell proliferation (PubMed:10374881). Phosphorylation on Tyr-454 is required for PTPN6 interaction, Tyr-426 for PTPN11 (By similarity). Tyr-426 is also required for SOCS3 binding, but Tyr-454/Tyr-456 motif is the preferred binding site (PubMed:12027890).
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Previously labelled as EPO Receptor.
Erythropoietin receptor (EPO-R) also known as EPOR plays an important role in erythropoiesis by mediating the effects of erythropoietin (EPO). EPO-R is a member of the cytokine receptor family with a mass of approximately 55 kDa. This receptor can primarily be found on the surface of erythroid progenitor cells in the bone marrow. Its presence is important for the final differentiation of these cells into mature erythrocytes.
EPO-R functions by dimerizing upon EPO binding subsequently activating intracellular signaling pathways. It is a component of a larger signaling complex that recruits and activates various molecules initiating a cascade of events critical for cell survival and proliferation. This receptor signaling prevents apoptosis in erythroid progenitor cells promoting their growth and differentiation into red blood cells.
EPO-R's activity falls within the JAK-STAT and PI3K-AKT signaling pathways. These pathways are pivotal in regulating hematopoiesis and cell survival. JAK2 acts as a direct partner to EPO-R and transduces the signal downstream while molecules like STAT5 get phosphorylated and mediate transcription of target genes. The PI3K-AKT pathway also contributes to the anti-apoptotic effect essential for erythrocyte development.
Altered EPO-R signaling associates with anemia of chronic disease and polycythemia vera. Anemic conditions often show reduced sensitivity or expression of EPO-R while mutations leading to EPO-R hypersensitivity link to polycythemia vera. Dysregulation of related proteins such as JAK2 also contributes to these conditions indicating the interconnected roles of these proteins in blood-related diseases.
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15% SDS-PAGE analysis of 3 μg ab219430.
Molecular Weight: 28-40 kDa (SDS-PAGE under reducing conditions).
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